Header list of 2flj.pdb file
Complete list - r 9 2 Bytes
HEADER LIPID BINDING PROTEIN 06-JAN-06 2FLJ TITLE FATTY ACID BINDING PROTEIN FROM LOCUST FLIGHT MUSCLE IN COMPLEX WITH TITLE 2 OLEATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LM-FABP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LOCUSTA MIGRATORIA; SOURCE 3 ORGANISM_COMMON: MIGRATORY LOCUST; SOURCE 4 ORGANISM_TAXID: 7004; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-3D KEYWDS FATTY ACID CARRIER, INTRACELLULAR LIPID BINDING PROTEIN, INVERTEBRATE KEYWDS 2 FABP, PROTEIN-LIGAND COMPLEX, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR C.LUECKE,Y.QIAO,H.T.B.VAN MOERKERK,J.H.VEERKAMP,J.A.HAMILTON REVDAT 3 09-MAR-22 2FLJ 1 REMARK SEQADV REVDAT 2 24-FEB-09 2FLJ 1 VERSN REVDAT 1 23-MAY-06 2FLJ 0 JRNL AUTH C.LUCKE,Y.QIAO,H.T.VAN MOERKERK,J.H.VEERKAMP,J.A.HAMILTON JRNL TITL FATTY-ACID-BINDING PROTEIN FROM THE FLIGHT MUSCLE OF LOCUSTA JRNL TITL 2 MIGRATORIA: EVOLUTIONARY VARIATIONS IN FATTY ACID BINDING. JRNL REF BIOCHEMISTRY V. 45 6296 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16700541 JRNL DOI 10.1021/BI060224F REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, DISCOVER 2000 REMARK 3 AUTHORS : ACCELRYS INC. (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FLJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-06. REMARK 100 THE DEPOSITION ID IS D_1000036022. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM LM-FABP COMPLEXED WITH U-13C REMARK 210 POTASSIUM OLEATE, 20 MM REMARK 210 PHOSPHATE BUFFER, 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 2D 1H-13C REMARK 210 HSQC; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 2.5.9, DISCOVER 2000 REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 26 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LAST MD STEPS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 25 REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-25 REMARK 465 RES C SSSEQI REMARK 465 MET A 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HD11 LEU A 46 HB2 LYS A 52 1.28 REMARK 500 OE1 GLU A 74 HG SER A 84 1.37 REMARK 500 HG1 THR A 76 OD1 ASP A 78 1.40 REMARK 500 H ASP A 12 O ILE A 129 1.46 REMARK 500 O LYS A 8 H GLN A 133 1.55 REMARK 500 H GLY A 69 O ILE A 86 1.55 REMARK 500 OD2 ASP A 78 HE ARG A 80 1.57 REMARK 500 O SER A 13 H ILE A 129 1.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 2 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 3 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 4 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 5 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 6 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 7 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 8 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 8 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 9 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 9 HIS A 102 CG HIS A 102 CD2 0.055 REMARK 500 10 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 10 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 11 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 12 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 12 HIS A 102 CG HIS A 102 CD2 0.055 REMARK 500 13 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 14 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 14 HIS A 102 CG HIS A 102 CD2 0.055 REMARK 500 15 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 15 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 16 HIS A 96 CG HIS A 96 CD2 0.056 REMARK 500 17 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 18 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 19 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 19 HIS A 102 CG HIS A 102 CD2 0.055 REMARK 500 20 HIS A 96 CG HIS A 96 CD2 0.056 REMARK 500 20 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 21 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 22 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 22 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 23 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 23 HIS A 102 CG HIS A 102 CD2 0.054 REMARK 500 24 HIS A 96 CG HIS A 96 CD2 0.055 REMARK 500 25 HIS A 96 CG HIS A 96 CD2 0.056 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 MET A 21 N - CA - CB ANGL. DEV. = -11.8 DEGREES REMARK 500 1 VAL A 26 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 1 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES REMARK 500 1 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 1 LEU A 77 CB - CA - C ANGL. DEV. = 14.0 DEGREES REMARK 500 1 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 1 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 1 HIS A 96 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 1 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 2 MET A 21 CB - CA - C ANGL. DEV. = 12.5 DEGREES REMARK 500 2 VAL A 26 CB - CA - C ANGL. DEV. = 13.1 DEGREES REMARK 500 2 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES REMARK 500 2 LEU A 77 CB - CA - C ANGL. DEV. = 14.1 DEGREES REMARK 500 2 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 HIS A 96 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 2 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 2 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 3 MET A 21 CA - CB - CG ANGL. DEV. = 10.5 DEGREES REMARK 500 3 VAL A 26 CB - CA - C ANGL. DEV. = 12.7 DEGREES REMARK 500 3 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES REMARK 500 3 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 3 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 3 LEU A 77 CB - CA - C ANGL. DEV. = 13.1 DEGREES REMARK 500 3 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 HIS A 96 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 3 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 3 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 4 VAL A 26 CB - CA - C ANGL. DEV. = 12.2 DEGREES REMARK 500 4 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES REMARK 500 4 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 4 LEU A 77 CB - CA - C ANGL. DEV. = 13.9 DEGREES REMARK 500 4 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 HIS A 96 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 4 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 4 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 5 VAL A 26 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 5 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES REMARK 500 5 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 5 LEU A 77 CB - CA - C ANGL. DEV. = 13.6 DEGREES REMARK 500 5 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 5 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 5 HIS A 96 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 5 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 5 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 6 MET A 21 N - CA - CB ANGL. DEV. = -12.0 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 254 ANGLE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 1 LEU A 46 -163.87 -104.00 REMARK 500 2 LEU A 46 -163.88 -103.93 REMARK 500 3 LEU A 46 -163.88 -103.91 REMARK 500 4 LEU A 46 -163.85 -103.93 REMARK 500 5 LEU A 46 -163.88 -103.89 REMARK 500 6 LEU A 46 -163.88 -103.93 REMARK 500 7 LEU A 46 -163.88 -103.93 REMARK 500 8 LEU A 46 -163.85 -103.89 REMARK 500 9 LEU A 46 -163.88 -103.93 REMARK 500 10 LEU A 46 -163.84 -104.00 REMARK 500 11 LEU A 46 -163.84 -103.98 REMARK 500 12 LEU A 46 -163.84 -104.00 REMARK 500 13 LEU A 46 -163.84 -104.00 REMARK 500 14 LEU A 46 -163.87 -104.00 REMARK 500 15 LEU A 46 -163.84 -103.94 REMARK 500 16 LEU A 46 -163.88 -103.91 REMARK 500 17 LEU A 46 -163.87 -104.00 REMARK 500 18 LEU A 46 -163.88 -103.93 REMARK 500 19 LEU A 46 -163.88 -103.91 REMARK 500 20 LEU A 46 -163.84 -103.95 REMARK 500 21 LEU A 46 -163.88 -103.98 REMARK 500 22 LEU A 46 -163.88 -103.95 REMARK 500 23 LEU A 46 -163.87 -103.96 REMARK 500 24 LEU A 46 -163.88 -103.98 REMARK 500 25 LEU A 46 -163.88 -103.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 TYR A 20 0.07 SIDE CHAIN REMARK 500 1 ARG A 80 0.12 SIDE CHAIN REMARK 500 1 ARG A 128 0.12 SIDE CHAIN REMARK 500 2 TYR A 20 0.07 SIDE CHAIN REMARK 500 2 ARG A 80 0.12 SIDE CHAIN REMARK 500 2 ARG A 128 0.12 SIDE CHAIN REMARK 500 3 TYR A 20 0.07 SIDE CHAIN REMARK 500 3 ARG A 80 0.13 SIDE CHAIN REMARK 500 3 ARG A 128 0.13 SIDE CHAIN REMARK 500 4 TYR A 20 0.07 SIDE CHAIN REMARK 500 4 ARG A 80 0.13 SIDE CHAIN REMARK 500 4 ARG A 128 0.11 SIDE CHAIN REMARK 500 5 ARG A 80 0.12 SIDE CHAIN REMARK 500 5 ARG A 128 0.13 SIDE CHAIN REMARK 500 6 ARG A 80 0.12 SIDE CHAIN REMARK 500 6 ARG A 128 0.13 SIDE CHAIN REMARK 500 7 TYR A 20 0.07 SIDE CHAIN REMARK 500 7 ARG A 80 0.12 SIDE CHAIN REMARK 500 7 ARG A 128 0.12 SIDE CHAIN REMARK 500 8 TYR A 20 0.07 SIDE CHAIN REMARK 500 8 ARG A 80 0.12 SIDE CHAIN REMARK 500 8 ARG A 128 0.12 SIDE CHAIN REMARK 500 9 ARG A 80 0.12 SIDE CHAIN REMARK 500 9 ARG A 128 0.13 SIDE CHAIN REMARK 500 10 ARG A 80 0.12 SIDE CHAIN REMARK 500 10 ARG A 128 0.11 SIDE CHAIN REMARK 500 11 TYR A 20 0.07 SIDE CHAIN REMARK 500 11 ARG A 80 0.13 SIDE CHAIN REMARK 500 11 ARG A 128 0.12 SIDE CHAIN REMARK 500 12 TYR A 20 0.07 SIDE CHAIN REMARK 500 12 ARG A 80 0.12 SIDE CHAIN REMARK 500 12 ARG A 128 0.12 SIDE CHAIN REMARK 500 13 ARG A 80 0.13 SIDE CHAIN REMARK 500 13 ARG A 128 0.13 SIDE CHAIN REMARK 500 14 ARG A 80 0.12 SIDE CHAIN REMARK 500 14 ARG A 128 0.13 SIDE CHAIN REMARK 500 15 TYR A 20 0.07 SIDE CHAIN REMARK 500 15 ARG A 80 0.12 SIDE CHAIN REMARK 500 15 ARG A 128 0.12 SIDE CHAIN REMARK 500 16 TYR A 20 0.07 SIDE CHAIN REMARK 500 16 ARG A 80 0.12 SIDE CHAIN REMARK 500 16 ARG A 128 0.13 SIDE CHAIN REMARK 500 17 TYR A 20 0.07 SIDE CHAIN REMARK 500 17 ARG A 80 0.12 SIDE CHAIN REMARK 500 17 ARG A 128 0.12 SIDE CHAIN REMARK 500 18 TYR A 20 0.10 SIDE CHAIN REMARK 500 18 ARG A 80 0.13 SIDE CHAIN REMARK 500 18 ARG A 128 0.13 SIDE CHAIN REMARK 500 19 TYR A 20 0.07 SIDE CHAIN REMARK 500 19 ARG A 80 0.12 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 70 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 POTASSIUM OLEATE, C18H33O2KA, A POTASSIUM SALT OF OLEIC REMARK 600 ACID WAS USED IN THE EXPERIMENTS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 134 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FTP RELATED DB: PDB REMARK 900 X-RAY STRUCTURE COORDINATES OF MUSCLE FATTY-ACID-BINDING PROTEIN REMARK 900 ISOLATED FROM THE DESERT LOCUST, SCHISTOCERCA GREGARIA REMARK 900 RELATED ID: 6931 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS OF THE LM-FABP:OLEATE COMPLEX DBREF 2FLJ A 1 133 UNP P41509 FABPM_LOCMI 1 133 SEQADV 2FLJ MET A 0 UNP P41509 INITIATING METHIONINE SEQRES 1 A 134 MET VAL LYS GLU PHE ALA GLY ILE LYS TYR LYS LEU ASP SEQRES 2 A 134 SER GLN THR ASN PHE GLU GLU TYR MET LYS ALA ILE GLY SEQRES 3 A 134 VAL GLY ALA ILE GLU ARG LYS ALA GLY LEU ALA LEU SER SEQRES 4 A 134 PRO VAL ILE GLU LEU GLU VAL LEU ASP GLY ASP LYS PHE SEQRES 5 A 134 LYS LEU THR SER LYS THR ALA ILE LYS ASN THR GLU PHE SEQRES 6 A 134 THR PHE LYS LEU GLY GLU GLU PHE ASP GLU ASP THR LEU SEQRES 7 A 134 ASP GLY ARG LYS VAL LYS SER ILE ILE THR GLN ASP GLY SEQRES 8 A 134 PRO ASN LYS LEU VAL HIS GLU GLN LYS GLY ASP HIS PRO SEQRES 9 A 134 THR ILE ILE ILE ARG GLU PHE SER LYS GLU GLN CYS VAL SEQRES 10 A 134 ILE THR ILE LYS LEU GLY ASP LEU VAL ALA THR ARG ILE SEQRES 11 A 134 TYR LYS ALA GLN HET OLA A 134 53 HETNAM OLA OLEIC ACID FORMUL 2 OLA C18 H34 O2 HELIX 1 1 VAL A 1 ALA A 5 5 5 HELIX 2 2 ASN A 16 ILE A 24 1 9 HELIX 3 3 GLY A 27 LEU A 37 1 11 SHEET 1 A10 ASN A 61 LYS A 67 0 SHEET 2 A10 LYS A 50 LYS A 56 -1 N SER A 55 O THR A 62 SHEET 3 A10 VAL A 40 VAL A 45 -1 N GLU A 44 O LYS A 52 SHEET 4 A10 LYS A 8 THR A 15 -1 N TYR A 9 O ILE A 41 SHEET 5 A10 LEU A 124 ALA A 132 -1 O ILE A 129 N ASP A 12 SHEET 6 A10 GLN A 114 LEU A 121 -1 N ILE A 119 O ALA A 126 SHEET 7 A10 THR A 104 PHE A 110 -1 N GLU A 109 O VAL A 116 SHEET 8 A10 LYS A 93 GLN A 98 -1 N HIS A 96 O ILE A 106 SHEET 9 A10 LYS A 81 GLN A 88 -1 N THR A 87 O VAL A 95 SHEET 10 A10 PHE A 72 ASP A 75 -1 N PHE A 72 O SER A 84 SITE 1 AC1 11 PHE A 17 TYR A 20 MET A 21 ILE A 24 SITE 2 AC1 11 VAL A 26 ILE A 59 LEU A 77 ARG A 108 SITE 3 AC1 11 ILE A 117 ARG A 128 TYR A 130 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - r 9 2 Bytes